FUNCTION:Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with dnaC protein, primase, and other prepriming proteins.
SUBUNIT:Homohexamer.
SIMILARITY:Belongs to the helicase family. DnaB subfamily.
Heat shock protein 70, Heat shock 70 kDa protein, HSP70
- Gene name
OrderedLocusNames=b0014, c0019, z0014, ECs0014;
- Comments
FUNCTION:Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the dnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the dnaA protein. Also participates actively in the response to hyperosmotic shock.
PTM:Autophosphorylated; grpE inhibits the autophosphorylation.
MISCELLANEOUS:The mutants dnaK756(Ts), seg-1 and seg-2 confer temperature sensitivity.
SIMILARITY:Belongs to the heat shock protein 70 family.
FUNCTION:Interacts with dnaK to disassemble a protein complex at the phage lambda origin of replication. Stimulates, jointly with grpE, the ATPase activity of dnaK.
COFACTOR:Binds 2 zinc ions per monomer.
SUBUNIT:Homodimer.
SUBCELLULAR LOCATION:Cytoplasmic.
INDUCTION:By heat shock under the control of the htpR regulatory protein.
Proc Natl Acad Sci U S A. 1971;68:2977-2981
Bacterial mutants in which the gene N function of bacteriophage lambda is blocked have an altered RNA polymerase.
Georgopoulos, C.
J Biol Chem. 1996;271:30798-30803
Role of the heat shock protein DnaJ in the lon-dependent degradation of naturally unstable proteins.
Jubete, Y., M. R. Maurizi, and S. Gottesman.
J Biol Chem. 1986;261:1782-1785
The nucleotide sequence of the Escherichia coli K12 and dnaJ+ gene: a gene that encodes a heat shock protein.
Bardwell, J. C., K. Tilly, E. A. Craig, J. King, M. Zylicz, and C. Georgopoulos.
J Biol Chem. 1986;261:1778-1781
Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.
Ohki, M., F. Tamura, S. Nishimura, and H. Uchida.
Biochim Biophys Acta. 1989;1009(1):94-8.
A complete deletion mutant of the Escherichia coli dnaKdnaJ operon.
Ohki R, Morita R, Kawamata T, Uchida H, Ohki M.
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2675977
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J Biol Chem. 1992;267:13180-13184
Escherichia coli dnaJ deletion mutation results in loss of stability of a positive regulator, CRP.
Ohki, R., T. Kawamata, Y. Katoh, F. Hosoda, and M. Ohki.
Eur J Biochem. 1973;35(2):331-7.
Biochemical and immunological characterization of threonyl-tRNA synthetase of two borrelidin-resistant mutants of Escherichia coli K12.
Paetz W, Nass G.
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4577856
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J Mol Biol. 1977;113(1):1-25.
Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12.
Saito H, Uchida H.
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328896
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Genes Dev. 1990;4:2202-2209
DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.
Straus, D., W. Walter, and C. A. Gross.
Mol Gen Genet. 1977;151(1):27-34.
A new host gene (groPC) necessary for lambda DNA replication.
Sunshine M, Feiss M, Stuart J, Yochem J.
(
325364
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Mol Gen Genet. 1983;192(1-2):10-4.
Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli.
Yamagata H, Taguchi N, Daishima K, Mizushima S.
(
6227793
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J Biol Chem. 1995;270:22669-22672
A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.
de Crouy-Chanel, A., M. Kohiyama, and G. Richarme.